Measles virus Hemagglutinin (H) and Fusion (F) glycoprotein (MeV H/F)

The Measles virus (MeV) surface antigens, specifically the Hemagglutinin (H) and Fusion (F) glycoproteins, are the primary mediators of viral entry into host cells. The H protein is responsible for recognizing and binding to specific host receptors, including CD150 (SLAM) on immune cells and Nectin-4 on epithelial cells (Citations: PubMed: 22016511, UniProt: P08362). Once bound, the H protein triggers the F protein to undergo a dramatic structural rearrangement that merges the viral and cellular membranes (Citations: PubMed: 21835787, UniProt: P03372). This process is essential for the delivery of the viral ribonucleoprotein complex into the host cytoplasm to initiate replication. These glycoproteins are the major targets for neutralizing antibodies induced by natural infection or vaccination with the live-attenuated measles vaccine (Citations: NIH: StatPearls - Measles). In addition to vaccines, these proteins are targets for experimental antiviral therapies, such as small-molecule fusion inhibitors like ERDRP-0519 and various monoclonal antibodies (Citations: PubMed: 25855243). Because they are exposed on the virion surface, they are also the primary site of selective pressure for the virus to evolve and escape immune detection. Understanding the interplay between H and F is crucial for developing treatments for severe measles complications, such as pneumonia and subacute sclerosing panencephalitis.

Other names

Measles virus surface antigensMeV H proteinMeV F proteinHemagglutininFusion glycoprotein

Neutralization of viral attachment by blocking Hemagglutinin-receptor interaction and inhibition of membrane fusion by preventing Fusion protein conformational changes.